Evidence map›Paper›PMID 25591178›Full record

ArticlePLoS biology2015

Composition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisome.

Andreas Diepold, Mikhail Kudryashev, Nicolas J Delalez, Richard M Berry, Judith P Armitage

Abstract read
In one paragraph

Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Targeting Type III Secretion System usingIndian journal of microbiology · 2025
    Review
  11. Article
  12. FEMS microbes · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Defining Assembly Pathways by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  20. Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Andreas DiepoldDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Mikhail KudryashevBiozentrum, University of Basel, Basel, Switzerland.
Nicolas J DelalezDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Richard M BerryClarendon Laboratory, Department of Physics, University of Oxford, Oxford, United Kingdom.
Judith P ArmitageDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.

Funding

Biotechnology and Biological Sciences Research Council BB/E00458X/1Biotechnology and Biological Sciences Research Council BB/H01991X/1Medical Research Council MR/K01577X/1Wellcome Trust 091911
6 · The paper itself

Abstract

Many gram-negative pathogens employ a type III secretion injectisome to translocate effector proteins into eukaryotic host cells. While the structure of the distal "needle complex" is well documented, the composition and role of the functionally important cytosolic complex remain less well understood. Using functional fluorescent fusions, we found that the C-ring, an essential and conserved cytosolic component of the system, is composed of ~22 copies of SctQ (YscQ in Yersinia enterocolitica), which require the presence of YscQC, the product of an internal translation initiation site in yscQ, for their cooperative assembly. Photoactivated localization microscopy (PALM) reveals that in vivo, YscQ is present in both a free-moving cytosolic and a stable injectisome-bound state. Notably, fluorescence recovery after photobleaching (FRAP) shows that YscQ exchanges between the injectisome and the cytosol, with a t½ of 68 ± 8 seconds when injectisomes are secreting. In contrast, the secretin SctC (YscC) and the major export apparatus component SctV (YscV) display minimal exchange. Under non-secreting conditions, the exchange rate of YscQ is reduced to t½ = 134 ± 16 seconds, revealing a correlation between C-ring exchange and injectisome activity, which indicates a possible role for C-ring stability in regulation of type III secretion. The stabilization of the C-ring depends on the presence of the functional ATPase SctN (YscN). These data provide new insights into the formation and composition of the injectisome and present a novel aspect of type III secretion, the exchange of C-ring subunits, which is regulated with respect to secretion.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsProtein BindingProtein StabilityProtein SubunitsProtein TransportType III Secretion SystemsYersinia enterocoliticaAdenosine TriphosphatasesBacterial ProteinsProtein SubunitsType III Secretion Systems

Identifiers

PMID25591178
PMCPMC4295842

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.